Search results for "Cellular Structures"

showing 7 items of 87 documents

The Lsm1-7/Pat1 complex binds to stress-activated mRNAs and modulates the response to hyperosmotic shock.

2018

RNA-binding proteins (RBPs) establish the cellular fate of a transcript, but an understanding of these processes has been limited by a lack of identified specific interactions between RNA and protein molecules. Using MS2 RNA tagging, we have purified proteins associated with individual mRNA species induced by osmotic stress, STL1 and GPD1. We found members of the Lsm1-7/Pat1 RBP complex to preferentially bind these mRNAs, relative to the non-stress induced mRNAs, HYP2 and ASH1. To assess the functional importance, we mutated components of the Lsm1-7/Pat1 RBP complex and analyzed the impact on expression of osmostress gene products. We observed a defect in global translation inhibition under…

Saccharomyces cerevisiae Proteinslcsh:QH426-470Gene ExpressionSaccharomyces cerevisiaeBiochemistryOsmotic PressureOsmotic ShockGeneticsRNA MessengerCellular Stress ResponsesGlycerol-3-Phosphate Dehydrogenase (NAD+)Biology and life sciencesMessenger RNAMembrane Transport ProteinsRNA-Binding ProteinsProteinsCell BiologyRepressor ProteinsNucleic acidslcsh:GeneticsRibonucleoproteinsRNA Cap-Binding ProteinsCell ProcessesProtein BiosynthesisPolyribosomesRNAProtein TranslationCellular Structures and OrganellesRibosomesProtein BindingResearch ArticlePLoS genetics
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Recovery Estimation of Dried Foodborne Pathogens Is Directly Related to Rehydration Kinetics.

2016

International audience; Drying is a common process which is used to preserve food products and technological microorganisms, but which is deleterious for the cells. The aim of this study is to differentiate the effects of drying alone from the effects of the successive and necessary rehydration. Rehydration of dried bacteria is a critical step already studied in starter culture but not for different kinetics and not for pathogens. In the present study, the influence of rehydration kinetics was investigated for three foodborne pathogens involved in neonatal diseases caused by the consumption of rehydrated milk powder: Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enteri…

Salmonella typhimuriumBacterial Diseases0301 basic medicineSurvivalPhysiologyMicroorganism[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritionCell MembranesResistancelcsh:MedicineEscherichia-coliPathology and Laboratory MedicineLactic Acid BacteriaFoodborne OrganismsSalmonellaMedicine and Health SciencesFood scienceProkaryoteslcsh:SciencemembraneMultidisciplinarybiologyDehydrationEnteric BacteriaSalmonella entericaBacterial InfectionsAnhydrobiosisBacterial PathogensDeathInfectious DiseasesMedical MicrobiologySalmonella entericaPathogensCellular Structures and OrganellesResearch ArticleWater activityDesiccation tolerance030106 microbiologyMicrobiologyMicrobiology03 medical and health sciencesCronobacter sakazakiiEnterobacteriaceaemedicineHumansDehydrationDesiccationMicrobial PathogensBacteriabusiness.industrylcsh:ROrganismsFood ConsumptionBiology and Life SciencesCell Biologymedicine.diseasebiology.organism_classificationFood safetyCronobacter sakazakiiInfant formulaFood MicrobiologyFluid Therapylcsh:QPhysiological ProcessesbusinessBacteriaWater activityPLoS ONE
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3D Morphology, ultrastructure and development of Ceratomyxa puntazzi stages: first insights into the mechanisms of motility and budding in the Myxozo…

2012

Free, amoeboid movement of organisms within media as well as substrate-dependent cellular crawling processes of cells and organisms require an actin cytoskeleton. This system is also involved in the cytokinetic processes of all eukaryotic cells. Myxozoan parasites are known for the disease they cause in economical important fishes. Usually, their pathology is related to rapid proliferation in the host. However, the sequences of their development are still poorly understood, especially with regard to pre-sporogonic proliferation mechanisms. The present work employs light microscopy (LM), electron microscopy (SEM, TEM) and confocal laser scanning microscopy (CLSM) in combination with specific…

SporesIndolesPhalloidineParasitic Diseases AnimalBiophysicsMotilitylcsh:MedicineBiologyBiochemistryFish DiseasesMicroscopy Electron TransmissionCell MovementMolecular Cell BiologyOxazinesAnimalsBilePseudopodiaMyxozoaCytoskeletonlcsh:ScienceBiologyCell ProliferationAmoeboid movementBuddingLife Cycle StagesMultidisciplinaryMicroscopy ConfocalStaining and LabelingPhysicslcsh:RProteinsCell BiologyActin cytoskeletonCellular StructuresSea BreamCell biologyUltrastructureMicroscopy Electron Scanninglcsh:QFilopodiaZoologyCytokinesisCell DivisionResearch ArticleDevelopmental BiologyPLoS ONE
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Chromatin modifiers and recombination factors promote a telomere fold-back structure, that is lost during replicative senescence.

2020

Telomeres have the ability to adopt a lariat conformation and hence, engage in long and short distance intra-chromosome interactions. Budding yeast telomeres were proposed to fold back into subtelomeric regions, but a robust assay to quantitatively characterize this structure has been lacking. Therefore, it is not well understood how the interactions between telomeres and non-telomeric regions are established and regulated. We employ a telomere chromosome conformation capture (Telo-3C) approach to directly analyze telomere folding and its maintenance in S. cerevisiae. We identify the histone modifiers Sir2, Sin3 and Set2 as critical regulators for telomere folding, which suggests that a dis…

TelomeraseProtein Folding:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::DNA-Binding Proteins::Rad52 DNA Repair and Recombination Protein [Medical Subject Headings]:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::Fungal Proteins::Saccharomyces cerevisiae Proteins [Medical Subject Headings]Gene ExpressionYeast and Fungal ModelsArtificial Gene Amplification and ExtensionQH426-470BiochemistryPolymerase Chain ReactionChromosome conformation captureHistonesCromatina0302 clinical medicineSirtuin 2Macromolecular Structure AnalysisSilent Information Regulator Proteins Saccharomyces cerevisiaeCellular Senescence:Organisms::Eukaryota::Fungi::Yeasts::Saccharomyces::Saccharomyces cerevisiae [Medical Subject Headings]0303 health sciencesChromosome BiologyEukaryota:Phenomena and Processes::Genetic Phenomena::Genetic Processes::DNA Replication [Medical Subject Headings]TelomereSubtelomere:Anatomy::Cells::Cellular Structures::Intracellular Space::Cell Nucleus::Cell Nucleus Structures::Intranuclear Space::Chromosomes::Chromosome Structures::Telomere [Medical Subject Headings]Chromatin3. Good healthChromatinCell biologyNucleic acidsTelomeres:Phenomena and Processes::Cell Physiological Phenomena::Cell Physiological Processes::Cell Cycle::Cell Division::Telomere Homeostasis [Medical Subject Headings]Experimental Organism SystemsDaño del ADNEpigeneticsResearch ArticleSenescenceDNA Replication:Chemicals and Drugs::Enzymes and Coenzymes::Enzymes::Hydrolases::Amidohydrolases::Histone Deacetylases [Medical Subject Headings]Chromosome Structure and FunctionProtein StructureSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeBiologyResearch and Analysis MethodsHistone DeacetylasesChromosomes03 medical and health sciencesSaccharomycesModel Organisms:Chemicals and Drugs::Enzymes and Coenzymes::Enzymes::Transferases::One-Carbon Group Transferases::Methyltransferases [Medical Subject Headings]:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::Intracellular Signaling Peptides and Proteins::Sirtuins::Sirtuin 2 [Medical Subject Headings]:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::Fungal Proteins::Saccharomyces cerevisiae Proteins::Silent Information Regulator Proteins Saccharomyces cerevisiae [Medical Subject Headings]DNA-binding proteinsGenetics:Chemicals and Drugs::Enzymes and Coenzymes::Enzymes::Recombinases::Rec A Recombinases::Rad51 Recombinase [Medical Subject Headings]Molecular Biology TechniquesMolecular Biology030304 developmental biologyCromosomasSenescencia celularOrganismsFungiBiology and Life SciencesProteinsTelomere HomeostasisCell BiologyDNAMethyltransferasesG2-M DNA damage checkpointProteína recombinante y reparadora de ADN Rad52YeastTelomereRad52 DNA Repair and Recombination ProteinRepressor ProteinsAnimal Studies:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::Transcription Factors::Repressor Proteins [Medical Subject Headings]DNA damageRad51 RecombinaseHomologous recombination030217 neurology & neurosurgeryTelómeroDNA DamagePLoS Genetics
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Transcriptional Activity and Nuclear Localization of Cabut, the Drosophila Ortholog of Vertebrate TGF-β-Inducible Early-Response Gene (TIEG) Proteins

2011

Background Cabut (Cbt) is a C2H2-class zinc finger transcription factor involved in embryonic dorsal closure, epithelial regeneration and other developmental processes in Drosophila melanogaster. Cbt orthologs have been identified in other Drosophila species and insects as well as in vertebrates. Indeed, Cbt is the Drosophila ortholog of the group of vertebrate proteins encoded by the TGF-s-inducible early-response genes (TIEGs), which belong to Sp1-like/Kruppel-like family of transcription factors. Several functional domains involved in transcriptional control and subcellular localization have been identified in the vertebrate TIEGs. However, little is known of whether these domains and fu…

Transcription GeneticNuclear Localization SignalsActive Transport Cell Nucleuslcsh:MedicineGene ExpressionBiochemistrybehavioral disciplines and activities03 medical and health sciencesModel Organisms0302 clinical medicineTransforming Growth Factor betaMolecular Cell Biologymental disordersGeneticsTranscriptional regulationAnimalsDrosophila Proteinslcsh:ScienceBiology030304 developmental biologyGeneticsZinc finger transcription factor0303 health sciencesMultidisciplinarybiologySchneider 2 cellslcsh:RfungiProteinsAnimal Modelsbiology.organism_classificationFusion proteinCellular StructuresDorsal closure3. Good healthRepressor ProteinsDrosophila melanogasterGene Expression RegulationVertebrateslcsh:QDrosophila melanogaster030217 neurology & neurosurgeryDrosophila ProteinNuclear localization sequenceTranscription FactorsResearch ArticleDevelopmental BiologyPLoS ONE
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PML nuclear body-residing proteins sequentially associate with HPV genome after infectious nuclear delivery.

2019

Subnuclear promyelocytic leukemia (PML) nuclear bodies (NBs) are targeted by many DNA viruses after nuclear delivery. PML protein is essential for formation of PML NBs. Sp100 and Small Ubiquitin-Like Modifier (SUMO) are also permanently residing within PML NBs. Often, large DNA viruses disassemble and reorganize PML NBs to counteract their intrinsic antiviral activity and support establishment of infection. However, human papillomavirus (HPV) requires PML protein to retain incoming viral DNA in the nucleus for subsequent efficient transcription. In contrast, Sp100 was identified as a restriction factor for HPV. These findings suggested that PML NBs are important regulators of early stages o…

Viral DiseasesPhysiologyvirusesIntranuclear Inclusion BodiesPromyelocytic Leukemia ProteinVirus ReplicationBiochemistryAutoantigensImmune PhysiologyMedicine and Health SciencesCell Cycle and Cell DivisionNuclear proteinBiology (General)PapillomaviridaeStaining0303 health sciencesViral GenomicsImmune System ProteinsChromosome Biology030302 biochemistry & molecular biologyCell StainingTotal Cell CountingNuclear Proteinsvirus diseasesAntigens NuclearGenomicsCell biologymedicine.anatomical_structureInfectious DiseasesCapsidCell ProcessesViral GenomeCellular Structures and OrganellesIntranuclear SpaceResearch ArticleHuman Papillomavirus InfectionQH301-705.5UrologyImmunologyCell Enumeration TechniquesSUMO-1 ProteinSexually Transmitted DiseasesMitosisMicrobial GenomicsGenome ViralBiologyResearch and Analysis MethodsMicrobiologyVirusAntibodies03 medical and health sciencesPromyelocytic leukemia proteinVirologyNuclear BodiesmedicineGeneticsHumansVesiclesMolecular BiologyMitosisTranscription factor030304 developmental biologyCell NucleusGenitourinary InfectionsTumor Suppressor ProteinsBiology and Life SciencesProteinsCell BiologyRC581-607Cell nucleusViral replicationSpecimen Preparation and Treatmentbiology.proteinParasitologyCapsid ProteinsImmunologic diseases. AllergyTranscription FactorsPLoS Pathogens
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Infection-induced chromatin modifications facilitate translocation of herpes simplex virus capsids to the inner nuclear membrane

2021

Herpes simplex virus capsids are assembled and packaged in the nucleus and move by diffusion through the nucleoplasm to the nuclear envelope for egress. Analyzing their motion provides conclusions not only on capsid transport but also on the properties of the nuclear environment during infection. We utilized live-cell imaging and single-particle tracking to characterize capsid motion relative to the host chromatin. The data indicate that as the chromatin was marginalized toward the nuclear envelope it presented a restrictive barrier to the capsids. However, later in infection this barrier became more permissive and the probability of capsids to enter the chromatin increased. Thus, although …

virusesGene ExpressionVirus ReplicationPathology and Laboratory Medicineherpes simplex -virusChlorocebus aethiopsCapsidsMedicine and Health SciencesSimplexvirusBiology (General)Mass DiffusivityStainingChromosome BiologyPhysicsChromatinChemistryMedical MicrobiologyViral PathogensPhysical SciencesVirusesHerpes Simplex Virus-1EpigeneticsCellular Structures and OrganellesPathogenskapsidiResearch ArticleHerpesvirusesNuclear EnvelopeQH301-705.5Biological Transport ActiveViral StructureResearch and Analysis MethodsinfektiotMicrobiologydiffuusio (fysikaaliset ilmiöt)CapsidNuclear MembraneVirologyGeneticsAnimalsherpesviruksetVero CellsMicrobial PathogensCell NucleusChemical PhysicsOrganismsBiology and Life SciencesHerpes SimplexCell Biologybiochemical phenomena metabolism and nutritionRC581-607Viral ReplicationHerpes Simplex VirusNuclear StainingSpecimen Preparation and TreatmentImmunologic diseases. AllergyDNA viruses
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